Plasma cells are terminally differentiated, non-proliferating cells, which secrete antibodies at very high rate (thousands of molecules per second corresponding to about 30-50 pg per cell per day).
The isolation of antibodies, for example monoclonal antibodies, from plasma cells relies on cloning and expression of the immunoglobulin genes. This can be done using phage display libraries of scrambled VH and VL genes isolated from plasma cells, or, by isolation of paired VH and VL genes from single plasma cells using single cell PCR. However, in order to screen the antibodies produced by plasma cells the immunoglobulin genes need to be cloned and expressed in a recombinant form in order to determine specificity and functional properties of the encoded antibody. This method is cumbersome, expensive, time-consuming, not adaptable to high-throughput and inefficient at retrieving rare antibodies that are produced by a minor fraction of the total repertoire of plasma cells.
Accordingly, there is a need to identify a more efficient method that is adaptable to high-throughput for the isolation and screening of antibodies, for example monoclonal antibodies, from plasma cells.